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Database: UniProt
Entry: Q1JL27
LinkDB: Q1JL27
Original site: Q1JL27 
ID   DDL_STRPC               Reviewed;         348 AA.
AC   Q1JL27;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   29-OCT-2014, entry version 63.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00047};
DE            EC=6.3.2.4 {ECO:0000255|HAMAP-Rule:MF_00047};
DE   AltName: Full=D-Ala-D-Ala ligase {ECO:0000255|HAMAP-Rule:MF_00047};
DE   AltName: Full=D-alanylalanine synthetase {ECO:0000255|HAMAP-Rule:MF_00047};
GN   Name=ddl {ECO:0000255|HAMAP-Rule:MF_00047};
GN   OrderedLocusNames=MGAS9429_Spy1205;
OS   Streptococcus pyogenes serotype M12 (strain MGAS9429).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=370551;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS9429;
RX   PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA   Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F.,
RA   DeLeo F.R., Musser J.M.;
RT   "Molecular genetic anatomy of inter- and intraserotype variation in
RT   the human bacterial pathogen group A Streptococcus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00047}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC       alanyl-D-alanine. {ECO:0000255|HAMAP-Rule:MF_00047}.
CC   -!- COFACTOR: Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000250}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00047}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00047}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00047}.
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|HAMAP-
CC       Rule:MF_00047}.
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DR   EMBL; CP000259; ABF32392.1; -; Genomic_DNA.
DR   RefSeq; YP_596936.1; NC_008021.1.
DR   ProteinModelPortal; Q1JL27; -.
DR   STRING; 370551.MGAS9429_Spy1205; -.
DR   EnsemblBacteria; ABF32392; ABF32392; MGAS9429_Spy1205.
DR   GeneID; 4061939; -.
DR   KEGG; spk:MGAS9429_Spy1205; -.
DR   PATRIC; 19753463; VBIStrPyo37061_1221.
DR   eggNOG; COG1181; -.
DR   HOGENOM; HOG000011593; -.
DR   KO; K01921; -.
DR   OMA; KLAFQYD; -.
DR   OrthoDB; EOG64BQ73; -.
DR   BioCyc; SPYO370551:GHLY-1264-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.30.470.20; -; 2.
DR   Gene3D; 3.40.50.20; -; 1.
DR   HAMAP; MF_00047; Dala_Dala_lig; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR000291; D-Ala_lig_Van_CS.
DR   InterPro; IPR005905; D_ala_D_ala.
DR   InterPro; IPR011095; Dala_Dala_lig_C.
DR   InterPro; IPR011127; Dala_Dala_lig_N.
DR   InterPro; IPR016185; PreATP-grasp_dom.
DR   PANTHER; PTHR23132; PTHR23132; 1.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF01820; Dala_Dala_lig_N; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01205; D_ala_D_alaTIGR; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00843; DALA_DALA_LIGASE_1; 1.
DR   PROSITE; PS00844; DALA_DALA_LIGASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell shape; Cell wall biogenesis/degradation;
KW   Complete proteome; Cytoplasm; Ligase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Peptidoglycan synthesis.
FT   CHAIN         1    348       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_1000030501.
FT   DOMAIN      132    334       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     162    217       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       288    288       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       301    301       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       301    301       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       303    303       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ   SEQUENCE   348 AA;  38969 MW;  BC221F78EBD31314 CRC64;
     MSKQTLVLLY GGRSAEREVS VLSAESVMRA VNYDKFLVKT YFITQMGQFI KTQQFSEKPS
     ESERLMTNET IELTQKIKPS DIYEEGAVVF PVLHGPMGED GSIQGFLEVL RMPYIGTNVM
     SSSIAMDKIT TKRVLESIGI PQVAYTVYID GQDLEACLVE TLARLTFPIF VKPANMGSSV
     GISKAQTKVE LRKAIQLALT YDSRVLIEQG VVAREIEVGL LGNDKVKSTL PGEVIKDVDF
     YDYQAKYVDN KITMAIPADV DQSIVTEMRS YAEVAFKALG GCGLSRCDFF LTQDGQVYLN
     ELNTMPGFTQ WSMYPLLWEN MGLAYPDLIE ELVTLAQEMF DQRESHLI
//
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